1hti

About this Structure
1HTI is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference
Page seeded by OCA on Wed Feb 18 06:38:05 2009

Derivation
As mentioned above, 1HTI comes from Homo sapiens; the functional annotation is given at the end of this page. The followings are some homologies according to the BLAST results(http://www.uniprot.org/blast/). The configurations are:

<1>Matrix: blosum62 <2>Threshold: 10  <3>Filtered: false  <4>Gapped: true  <5>Maximum number of hits reported: 250  <6>Database: uniprotkb (Protein) generated for BLAST on Nov 2, 2010

Accession  Entry_Name     Organism                     GO IDs and terms D3DUS9     D3DUS9_HUMAN   Homo sapiens                 0005975  carbohydrate metabolic process 0006006 glucose metabolic process 0003824 catalytic activity 0004807 triose-phosphate isomerase activity 0005625 soluble fraction 0005634 nucleus P60175     TPIS_PANTR     Pan troglodytes              0006006  glucose metabolic process 0006094 gluconeogenesis 0003824 catalytic activity 0004807 triose-phosphate isomerase activity P60174     TPIS_HUMAN     Homo sapiens                 0005975  carbohydrate metabolic process 0006006 glucose metabolic process 0003824 catalytic activity 0004807 triose-phosphate isomerase activity 0005625 soluble fraction 0005634 nucleus P00939     TPIS_RABIT     Oryctolagus cuniculus(Rabbit)0006006  glucose metabolic process 0006094 gluconeogenesis 0003824 catalytic activity 0004807 triose-phosphate isomerase activity P15426     TPIS_MACMU     Macaca mulatta               0006094  gluconeogenesis 0006096 glycolysis 0003824 catalytic activity 0004807 triose-phosphate isomerase activity ... ...

What's New~
"Triosephosphate isomerase (TIM) is a perfectly evolved enzyme...Researchers continue to use TIM as a study object for their research, both for computational enzyme mechanism studies as well as for experimental studies."

--R. K. Wierenga, E. G. Kapetaniou and R. Venkatesan, "Triosephosphate isomerase: a highly evolved biocatalyst", Cell Mol Life Sci. 2010 Dec

"In the present study, we theoretically assessed the effects of 20 point mutations detected previously in a region of the triose-phosphate  isomerase gene (tpi) of the protozoan Giardia duodenalis on the three-dimensional structure of the ‘wild-type’ protein (TPI)...the findings   provide support for the “neutral theory”, which contends that evolution at the molecular level is not solely shaped by “Darwinian selection  but also by random drift of selectively neutral or nearly neutral mutants”."

--Nolan MJ, Hofmann A, Jex AR, Gasser RB, "A theoretical study to establish the relationship between the three-dimensional structure of triose-phosphate isomerase of Giardia duodenalis and point mutations in the respective gene", Mol Cell Probes. 2010 Oct

GO Functional Annotation
as TRIOSEPHOSPHATE ISOMERASE(reference: http://www.pdb.org/pdb/explore/explore.do?structureId=1HTI)

(1)Cellular component: GO_ID        GO_term 0005625      soluble fraction 0005634      nucleus 0005829        cytosol

(2)Biological process: GO_ID        GO_term 0008152      metabolic process 0007275      multicellular organismal development 0009790      embryonic development 0005975      carbohydrate metabolic process 0008610        lipid biosynthetic process 0019682          glyceraldehyde-3-phosphate metabolic process 0006633            fatty acid biosynthetic process 0006006              glucose metabolic process 0006094                gluconeogenesis 0006096          glycolysis 0006098          pentose-phosphate shunt (3)Biochemical function: GO_ID        GO_term 0003824      catalytic activity 0005515      protein binding 0016853      isomerase activity 0004807        triose-phosphate isomerase activity